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Database: UniProt
Entry: F2S9K8_TRIT1
LinkDB: F2S9K8_TRIT1
Original site: F2S9K8_TRIT1 
ID   F2S9K8_TRIT1            Unreviewed;      1029 AA.
AC   F2S9K8;
DT   31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   31-MAY-2011, sequence version 1.
DT   27-MAR-2024, entry version 62.
DE   RecName: Full=Rho guanyl nucleotide exchange factor {ECO:0008006|Google:ProtNLM};
DE   Flags: Fragment;
GN   ORFNames=TESG_07621 {ECO:0000313|EMBL:EGE00258.1};
OS   Trichophyton tonsurans (strain CBS 112818) (Scalp ringworm fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX   NCBI_TaxID=647933;
RN   [1] {ECO:0000313|EMBL:EGE00258.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 112818 {ECO:0000313|EMBL:EGE00258.1};
RG   The Broad Institute Genome Sequencing Platform;
RA   Cuomo C., Henn M., Martinez D., Young S.K., Zeng Q., Gargeya S., Haas B.,
RA   Alvarado L., Berlin A., Chapman S., Chen Z., Freedman E., Gellesch M.,
RA   Goldberg J., Griggs A., Gujja S., Heilman E.R., Heiman D., Howarth C.,
RA   Larson L., Mehta T., Pearson M., Roberts A., Saif S., Shea T., Shenoy N.,
RA   Sisk P., Stolte C., Sykes S., White J., Yandava C., White T.C.,
RA   Abdel-Rahman S., Graser Y., Gurr S.J., Kohler G., Martinez-Rossi N.,
RA   Oliver B.C., Rossi A., Shelest E., Summerbell R., Lander E., Nusbaum C.,
RA   Birren B.;
RT   "Annotation of Trichophyton tonsurans strain CBS 112818.";
RL   Submitted (JUL-2009) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; GG698535; EGE00258.1; -; Genomic_DNA.
DR   AlphaFoldDB; F2S9K8; -.
DR   HOGENOM; CLU_007879_1_0_1; -.
DR   OrthoDB; 23973at2759; -.
DR   Proteomes; UP000009172; Unassembled WGS sequence.
DR   GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IEA:InterPro.
DR   CDD; cd05992; PB1; 1.
DR   CDD; cd13246; PH_Scd1; 1.
DR   CDD; cd00160; RhoGEF; 1.
DR   Gene3D; 1.20.900.10; Dbl homology (DH) domain; 1.
DR   Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR   InterPro; IPR010481; Cdc24/Scd1_N.
DR   InterPro; IPR033511; Cdc24/Scd1_PH_dom.
DR   InterPro; IPR035899; DBL_dom_sf.
DR   InterPro; IPR000219; DH-domain.
DR   InterPro; IPR000270; PB1_dom.
DR   InterPro; IPR011993; PH-like_dom_sf.
DR   PANTHER; PTHR47339; CELL DIVISION CONTROL PROTEIN 24; 1.
DR   PANTHER; PTHR47339:SF1; CELL DIVISION CONTROL PROTEIN 24; 1.
DR   Pfam; PF06395; CDC24; 1.
DR   Pfam; PF00564; PB1; 1.
DR   Pfam; PF15411; PH_10; 1.
DR   Pfam; PF00621; RhoGEF; 1.
DR   SMART; SM00325; RhoGEF; 1.
DR   SUPFAM; SSF54277; CAD & PB1 domains; 1.
DR   SUPFAM; SSF48065; DBL homology domain (DH-domain); 1.
DR   SUPFAM; SSF50729; PH domain-like; 1.
DR   PROSITE; PS50010; DH_2; 1.
DR   PROSITE; PS51745; PB1; 1.
PE   4: Predicted;
FT   DOMAIN          179..358
FT                   /note="DH"
FT                   /evidence="ECO:0000259|PROSITE:PS50010"
FT   DOMAIN          929..1027
FT                   /note="PB1"
FT                   /evidence="ECO:0000259|PROSITE:PS51745"
FT   REGION          600..929
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        613..632
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        643..679
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        717..752
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        765..812
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        854..883
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:EGE00258.1"
SQ   SEQUENCE   1029 AA;  115620 MW;  DADBBAF170E664C3 CRC64;
     AKMEGMNGNH IMAEDNIINR RGGESLFQNC SNLKKRLAEV PGFEPHLAEM QELDKASDEN
     DPVASVWKCL RQGYPLMTIY NATHPSEPLS IDENKLQERN RPKAATFKFL QACLQVLKFP
     QQECFLITDL YGDSTTGFVK VIKMVNRVID ILELQGQLYN KVSPSTSLPS EGGKTKLTRR
     EHILKEMLET ERDYVHHLQN LQALKKELEE TGALTGDVSH QIFLNLNNLL DFTQRFLIRM
     EQHNALPEET QNWGDLYLSH HNGFLQYEPF IANQPRCDQI CQREWDKIHS APRSPDLQQM
     VAQLSTLNGF FVKPFQRLTK YPLMLMELRK QTENPGLVSD ISEAINMIQI ILDNANRAID
     KEHLVSAVED LSQRVEDWKA LKLDQFGDLL RYGTFTILKG DSGKDAEREV RIILSNTTAQ
     SYLLGSRRKS FTGSVIHLLS ANSHRSWSWK QPKDTKYISV CPTPTQVAHP LELLTPTHSA
     STKTLEFNTP PPRPWTRLYH IYLFEQILLC CKDIYPAKQK SKLMGKEKVV PNPKVKPKLQ
     LKGRIYMTNV TEILSLSKPG SYKIQIFWKG DPGVVDNFGI RYRDEDTMNK WYKDIDKQRA
     LQTHERPSSK NHGTSETEFT YLRNTPKPPN PYQEEYSTEE ELSREPTNTS LSEFSTSRNA
     SNTSLRGRSA TNGSGGSGHH SGGRPQFPTP NAPLTVHTQF APGAVSPGER NGASYFSPTG
     EAPSSTRSSS QSTAFSYSRG GTPSNAWTEA EQNRYTAPAM PRSGSRDGSG NNPYYNNGSR
     NAQRPSLPPF SSNQNGQSGS QSQAQARMRS ASSPDIHNGA VPDSRRYMNG GHTMQTVDNV
     PVPPIPPHMA NMRAPVNRSQ NSSPTGNTIP IRSGTQSPNL QPPPSRHGHA HPPPVGYNYE
     PHAPNGRPLQ PPTSMPQTSP FDDPDSQMPS QLKAKINFDD NYVTLVIASN ILFRSLTDRV
     DAKLARFTDR SIGGNSARLR YRDEDGDFVT IDSDEAVQLA FMEWREQHQH SLAAGQVGEI
     QLFCQPVEN
//
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